The three things that can cause the enzyme to denature is a large change in pH level, High Temperature, and substrate concentration. According to our knowledge, we know that a large change in pH will cause instability in the protein structure thus resulting in denaturation of the enzyme. From the data, we can see that pH 3 (total:6.3) and 10 (total:6.2) were the slowest because pH 3 is probably the highest acid and pH 10 is the highest base. The highest acid or base pH represents a large change which would cause the enzyme to denature. The fastest pH was 6 (total:34.5), and it seems that there wasn’t a large change which resulted in a stable structure. The temperature in our experiment was not very high which didn’t result in denaturation of peroxidase. The temperature seemed to be a constant that didn’t affect the experiment. If the temperature was higher in pH 3 and low in pH 10, then it would cause pH 3 to denature even more which would make the pH 3 total about 4.0. Substrate concentration basically means the amount used for the substrate. The substrate in our experiment was 0.1% hydrogen peroxide. The 0.1% is the concentration amount. Just like temperature and pH, substrate concentration can speed the reaction only up to a certain limit. When we mixed pH 3 enzyme tube with substrate tube, we used 0.3 mL of hydrogen peroxide, but if we were to increase the amount, then the experiment would have been faster. Our
In this experiment it was found that increase in number of drops of enzyme suspension led to increased pressure as shown in the table 3. The reaction was repeated 3 times and average rate noted. From these rates a graph was plotted which describes the relationship of the pressure produced and number of drops added. The reaction rates were measured by Kpa/min and were written to 4 figures for precise results.
Enzymes are needed for survival in any living system and they control cellular reactions. Enzymes speed up chemical reactions by lowering the energy needed for molecules to begin reacting with each other. They do this by forming an enzyme-substrate complex that reduces energy that is required for a specific reaction to occur. Enzymes determine their functions by their shape and structure. Enzymes are made of amino acids, it 's made of anywhere from a hundred to a million amino acids, each they are bonded to other chemical bonds. The enzymeʼs have an active site that allows only certain substances to bind, they do this by having an enzyme and substrate that fit together perfectly. If the enzyme shape is changed then the binding
LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable pH 3. Controlled Variables temperature, amount of substrate (sucrose) present, sucrase + sucrose incubation time Effect of Temperature on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable temperature 3. Controlled Variables pH, amount of
Abstract: Enzymes can catalyze chemical reactions by speeding up the chemicals activation energy. Temperature and pH are just two of the factors that affects enzymes and their involvement with chemicals and the way they function. Throughout this experiment, we conducted a study on peroxidase, which is an enzyme. The following information consist of the recordings of when it was exposed to four different pH levels to come up with an optimum pH and IRV at the end.
The purpose of this experiment was to analyze the effects of the variables: temperature, pH, and enzyme concentration, on the enzymatic reaction rate of catalase and the level at which its products are released, measuring the rate of absorption using the indicator solution guaiacol and a spectrophotometer to develop a hypothesis of the ideal conditions for these reactions. My hypothesis is that the extremes in concentration, temperature and pH will negatively affect the Au rate. This experiment used 11 solutions contained in cuvettes. Each cuvette, once mixed, is placed in spectrophotometer and then a reading taken every 20 seconds. Cuvettes 1, 8, and 10 are used as blanks to zero out the spectrophotometer. They all lack the enzyme to help determine the absorption of just the enzyme.
To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds. It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect.
The purpose of quantitative analysis of protein using a spectrophotometer is to measure the concentration of proteins in a given sample. The experiment is conducted by laboratory method (Biuret Test) and using spectrophotometer to analyze the absorbance of reactants at 540 nm, hence determining the concentration of the proteins in a given sample.
Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1). These factors include the pH and the temperature of the solution (1). Most enzymes have a preferred temperature and pH range (2). The preferred temperature for catalase falls between the ranges of thirty five to fifty degrees Celsius (4). Temperatures that are too high denature the enzyme and halt the enzyme’s activity (2). Catalase denatures starts to denature at fifty five degrees Celsius (2). Reactions in the human body produce hydrogen peroxide as a product (1). Since hydrogen peroxide is poisonous to the human body, catalase catalyzes hydrogen peroxide into water and oxygen (2 H2O2 → 2 H2O + O2) (1). According to the collision theory, a reaction can only occur if particles collide with sufficient energy to overcome the activation energy and with correct geometrical orientation (3). Increasing temperature increases the kinetic energy of the particles which means that an increase in temperature will increase the speed of the hydrogen peroxide and the catalase molecules which
The purpose of this study is to investigate the effects of varying the concentration of peroxidase on rate of reaction, as well as, the varying temperature and pH levels. Enzymes are proteins that catalyze biochemical reactions that work by reducing the activation energy for each reaction, causing an increase to the rate of the reaction. One class of enzymes are known as peroxidase. Peroxidase catalyze the oxidation of a particular substrate by hydrogen peroxide. Meaning that it eliminates H2O2 in order to prevent damage to the cells and tissues (Department of Biology University of Tampa 74). Peroxidase is the most reliable and accessible enzyme to use as it can be easily prepared and tested (Ramesh Kumar 1). An enzymes shape is critical
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells. The 3 concentrations of enzymes were 0.5 ml, 1.0 ml, and 2.0 ml of turnip extract, while the substrate consisted of 0.1ml, 0.2 ml, and 0.4 ml of hydrogen peroxide. In a separate tube, the control was made up of turnip extract and guaiacol, known as the color reagent. This was recorded the absorbance every 20 seconds for 3 minutes.
Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration
Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan Man Jeun Duncan (16002621) Law Sze Man (16000478) Introduction Enzyme is a protein base structure substance in our body. It works at a biocatalyst that will catalyzing the chemical reaction, which helps to speed up the chemical reaction. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. The aim of this experiment is to see can the enzyme functions normally in different environment(pH, temperature and salt concentration) via using starch solution, amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and NaCl solution, and using iodine solution